lørdag den 21. januar 2017

Delta-1-pyrroline-5-carboxylate dehydrogenase, mitochondrial
is an enzyme that in humans is encoded by
the ALDH4A1 gene (aldehyde dehydrogenase 4 family, member A1). This enzyme is a mitochondrial matrix
NAD-dependent dehydrogenase that catalyzes the second
step of the proline degradation pathway, converting
pyrroline-5-carboxylate to glutamate. Deficiency of this
enzyme is associated with type II hyperprolinemia, an
autosomal recessive disorder characterized by accumulation
of delta-1-pyrroline-5-carboxylate (P5C) and proline. (1).

Pyrroline-5-carboxylic acid is increased in ME patients (2).

The gene ALDH4A1 has been found epigenetic changed (hypermethylated) in ME (3).

Expression of the proteins P5C-dehyrogenase and P5C-synthase have been found upregulated in ME (4).

P5C-dehydrogenase has been found to be an immunoreactive protein against IgGs from POTS-patients (5).

A proteomic study on cerebrospinal fluid from ME/CFS patients has shown an upregulation of the pathway "valine, leucine and isoleucine degradation" (table S6 in ref 2).

The gene acyl-CoA.dehydrogenase family member 8 (ACAD8) has been found epigenetic changed (hypermethylated) in ME (3).

ACAD8 is an isobutyryl-CoA dehydrogenase that functions in the catabolism of branched-chain amino acids including valine, and shows high reactivity toward isobutyryl-CoA. ACAD8 is responsible for the third step in the breakdown of valine and converts isobutyryl-CoA into methylacrylyl-CoA.